Structure of PDB 2e9f Chain B

Receptor sequence
>2e9fB (length=450) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
GPDALAARFNASLAFDRALWREDLWQNRVHARMLHAVGLLSAEELEAILK
GLDRIEEEIEAGTFPWREELEDVHMNLEARLTELVGPPGGKLHTARSRND
QVATDLRLYLRGAIDELLALLLALRRVLVREAEKHLDPLYVLPGYTHLQR
AQPVLLAHWFLAYYEMLKRDAGRLEDAKERLNESPLGAAALAGTGFPIDR
HFTARELGFKAPMRNSLDAVASRDFALEVLSALNIGMLHLSRMAEELILY
STEEFGFVEVPDAFATGSSIMPQKKNPDILELIRAKAGRVLGAFVGLSAV
VKGLPLAYNKDLQEDKEPLLDALATYRDSLRLLAALLPGLKWRRERMWRA
AEGGYTLATELADYLAEKGLPFREAHHVVGRLVRRLVEEGRALKDLTLEE
LQAHHPLFAEDALPLLRLETAIHRRRSYGGTAPEAVRERLEEAKKEVGLD
3D structure
PDB2e9f Crystal Structure of T.th.HB8 Argininosuccinate lyase complexed with L-Arginine
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E83 T158 H159 S280 S281 K286 E293
Catalytic site (residue number reindexed from 1) E71 T146 H147 S268 S269 K274 E281
Enzyme Commision number 4.3.2.1: argininosuccinate lyase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ARG B R110 N111 V114 Y320 Q325 K328 R98 N99 V102 Y308 Q313 K316
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004056 argininosuccinate lyase activity
GO:0016829 lyase activity
Biological Process
GO:0006526 L-arginine biosynthetic process
GO:0042450 arginine biosynthetic process via ornithine
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2e9f, PDBe:2e9f, PDBj:2e9f
PDBsum2e9f
PubMed
UniProtQ5SLL0|ARLY_THET8 Argininosuccinate lyase (Gene Name=argH)

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